UniProtKB - Q9UNL4 (ING4_HUMAN)
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- BLAST>sp|Q9UNL4|ING4_HUMAN Inhibitor of growth protein 4 OS=Homo sapiens OX=9606 GN=ING4 PE=1 SV=1 MAAGMYLEHYLDSIENLPFELQRNFQLMRDLDQRTEDLKAEIDKLATEYMSSARSLSSEE KLALLKQIQEAYGKCKEFGDDKVQLAMQTYEMVDKHIRRLDTDLARFEADLKEKQIESSD YDSSSSKGKKKGRTQKEKKAARARSKGKNSDEEAPKTAQKKLKLVRTSPEYGMPSVTFGS VHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPRGKWFCP RCSQERKKK
- Align
Inhibitor of growth protein 4
ING4
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
6 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity."
Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K., Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C.
Cancer Res. 63:2373-2378(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EP300 AND TP53. - Ref.8"ING4 induces G2/M cell cycle arrest and enhances the chemosensitivity to DNA-damage agents in HepG2 cells."
Zhang X., Xu L.-S., Wang Z.-Q., Wang K.-S., Li N., Cheng Z.-H., Huang S.-Z., Wei D.-Z., Han Z.-G.
FEBS Lett. 570:7-12(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.9"The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis."
Garkavtsev I., Kozin S.V., Chernova O., Xu L., Winkler F., Brown E., Barnett G.H., Jain R.K.
Nature 428:328-332(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RELA, SUBCELLULAR LOCATION. - Ref.10"A screen for genes that suppress loss of contact inhibition: Identification of ING4 as a candidate tumor suppressor gene in human cancer."
Kim S., Chin K., Gray J.W., Bishop J.M.
Proc. Natl. Acad. Sci. U.S.A. 101:16251-16256(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.12"The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF)."
Ozer A., Wu L.C., Bruick R.K.
Proc. Natl. Acad. Sci. U.S.A. 102:7481-7486(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH EGLN1. - Ref.13"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN HISTONE ACETYLATION, FUNCTION IN DNA REPLICATION, FUNCTION IN TP53-MEDIATED TRANSCRIPTION, IDENTIFICATION IN THE HBO1 COMPLEX.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 198 | Histone H3K4me3By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 199 | Zinc 1By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 201 | Zinc 1By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 209 | Histone H3K4me3By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 212 | Zinc 2By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 213 | Histone H3K4me3By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 217 | Zinc 2By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 221 | Histone H3K4me3By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 223 | Zinc 1; via pros nitrogenBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 226 | Zinc 1By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 239 | Zinc 2By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 242 | Zinc 2By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 196 – 245 | PHD-typePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 50 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- methylated histone binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription coactivator activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- apoptotic process Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cell cycle arrest Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- DNA replication Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- histone H3 acetylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- histone H4-K12 acetylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- histone H4-K5 acetylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- histone H4-K8 acetylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of cell proliferation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of growth Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of transcription, DNA-templated Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of apoptotic process Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein acetylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Chromatin regulator |
| Biological process | Apoptosis, Cell cycle |
| Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-3214847 HATs acetylate histones |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9UNL4 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Inhibitor of growth protein 4Alternative name(s): p29ING4 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:ING4 ORF Names:My036 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000111653.19 |
Human Gene Nomenclature Database More...HGNCi | HGNC:19423 ING4 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 608524 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UNL4 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- Nucleus 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Novel splice variants of ING4 and their possible roles in the regulation of cell growth and motility."
Unoki M., Shen J.C., Zheng Z.M., Harris C.C.
J. Biol. Chem. 281:34677-34686(2006) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 5; 6 AND 7), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING. - Ref.9"The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis."
Garkavtsev I., Kozin S.V., Chernova O., Xu L., Winkler F., Brown E., Barnett G.H., Jain R.K.
Nature 428:328-332(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RELA, SUBCELLULAR LOCATION.
- Nucleus 2 Publications
Cytoskeleton
- intermediate filament cytoskeleton Source: HPA
Cytosol
- cytosol Source: HPA
Nucleus
- histone acetyltransferase complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Tumor suppressorOrganism-specific databases
DisGeNET More...DisGeNETi | 51147 |
Open Targets More...OpenTargetsi | ENSG00000111653 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134976283 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ING4 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 57012981 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000212668 | 1 – 249 | Inhibitor of growth protein 4Add BLAST | 249 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 112 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 127 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 129 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 133 | Citrulline1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 146 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 148 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 156 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 166 | Citrulline1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| Isoform 4 (identifier: Q9UNL4-4) | |||||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 114 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 127 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"Citrullination of inhibitor of growth 4 (ING4) by peptidylarginine deminase 4 (PAD4) disrupts the interaction between ING4 and p53."
Guo Q., Fast W.
J. Biol. Chem. 286:17069-17078(2011) [PubMed] [Europe PMC] [Abstract]Cited for: CITRULLINATION AT ARG-133 AND ARG-166, NUCLEAR LOCALIZATION SIGNAL.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, CitrullinationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9UNL4 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UNL4 |
PeptideAtlas More...PeptideAtlasi | Q9UNL4 |
PRoteomics IDEntifications database More...PRIDEi | Q9UNL4 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 85303 85304 [Q9UNL4-2] 85305 [Q9UNL4-3] 85306 [Q9UNL4-4] 85307 [Q9UNL4-5] 85308 [Q9UNL4-6] 85309 [Q9UNL4-7] 85310 [Q9UNL4-8] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UNL4 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UNL4 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000111653 |
CleanEx database of gene expression profiles More...CleanExi | HS_ING4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UNL4 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UNL4 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA031817 HPA057338 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
8 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity."
Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K., Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C.
Cancer Res. 63:2373-2378(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EP300 AND TP53. - Ref.9"The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis."
Garkavtsev I., Kozin S.V., Chernova O., Xu L., Winkler F., Brown E., Barnett G.H., Jain R.K.
Nature 428:328-332(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RELA, SUBCELLULAR LOCATION. - Ref.12"The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF)."
Ozer A., Wu L.C., Bruick R.K.
Proc. Natl. Acad. Sci. U.S.A. 102:7481-7486(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH EGLN1. - Ref.13"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN HISTONE ACETYLATION, FUNCTION IN DNA REPLICATION, FUNCTION IN TP53-MEDIATED TRANSCRIPTION, IDENTIFICATION IN THE HBO1 COMPLEX. - Ref.14"ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression."
Shi X., Hong T., Walter K.L., Ewalt M., Michishita E., Hung T., Carney D., Pena P., Lan F., Kaadige M.R., Lacoste N., Cayrou C., Davrazou F., Saha A., Cairns B.R., Ayer D.E., Kutateladze T.G., Shi Y. , Cote J., Chua K.F., Gozani O.
Nature 442:96-99(2006) [PubMed] [Europe PMC] [Abstract]Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2. - Ref.17"Molecular basis of histone H3K4me3 recognition by ING4."
Palacios A., Munoz I.G., Pantoja-Uceda D., Marcaida M.J., Torres D., Martin-Garcia J.M., Luque I., Montoya G., Blanco F.J.
J. Biol. Chem. 283:15956-15964(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 188-245 IN COMPLEX WITH H3K4ME3, DOMAIN PHD, SUBUNIT. - Ref.18"ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation."
Hung T., Binda O., Champagne K.S., Kuo A.J., Johnson K., Chang H.Y., Simon M.D., Kutateladze T.G., Gozani O.
Mol. Cell 33:248-256(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 194-246, SUBUNIT. - Ref.19"Crystal structure of inhibitor of growth 4 (ING4) dimerization domain reveals functional organization of ING family of chromatin-binding proteins."
Culurgioni S., Munoz I.G., Moreno A., Palacios A., Villate M., Palmero I., Montoya G., Blanco F.J.
J. Biol. Chem. 287:10876-10884(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 2-105, COILED-COIL DOMAIN, SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| HIST1H3D | P68431 | 3 | EBI-2866661,EBI-79722 | |
| HNRNPD | Q14103 | 9 | EBI-2866661,EBI-299674 | |
| HNRNPD | Q14103-4 | 2 | EBI-2866661,EBI-432545 | |
| NAV2 | Q8IVL1 | 3 | EBI-2866661,EBI-741200 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- methylated histone binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 119331, 47 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-718 HBO1-4.1 histone acetyltransferase complex CPX-719 HBO1-4.2 histone acetyltransferase complex CPX-720 HBO1-4.3 histone acetyltransferase complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9UNL4 |
Database of interacting proteins More...DIPi | DIP-42222N |
Protein interaction database and analysis system More...IntActi | Q9UNL4, 30 interactors |
Molecular INTeraction database More...MINTi | Q9UNL4 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000380024 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 5 – 12 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 14 – 16 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 17 – 50 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 34 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 58 – 103 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 46 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 199 – 202 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 207 – 211 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 221 – 223 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 225 – 227 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 240 – 243 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 244 – 246 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UNL4 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UNL4 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9UNL4 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 25 – 118 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 94 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 127 – 148 | Bipartite nuclear localization signalAdd BLAST | 22 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Zinc finger
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 196 – 245 | PHD-typePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 50 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Coiled coil, Zinc-fingerPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1973 Eukaryota COG5034 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000074538 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000239724 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG006607 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UNL4 |
KEGG Orthology (KO) More...KOi | K11346 |
Identification of Orthologs from Complete Genome Data More...OMAi | PRCSQDR |
Database of Orthologous Groups More...OrthoDBi | EOG091G0J8Y |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UNL4 |
TreeFam database of animal gene trees More...TreeFami | TF352014 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.40.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR028647 ING4 IPR024610 ING_N_histone_binding IPR019786 Zinc_finger_PHD-type_CS IPR011011 Znf_FYVE_PHD IPR001965 Znf_PHD IPR019787 Znf_PHD-finger IPR013083 Znf_RING/FYVE/PHD |
The PANTHER Classification System More...PANTHERi | PTHR10333:SF40 PTHR10333:SF40, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF12998 ING, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01408 ING, 1 hit SM00249 PHD, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF57903 SSF57903, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01359 ZF_PHD_1, 1 hit PS50016 ZF_PHD_2, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (8)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 8 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKGKK KGRTQKEKKA ARARSKGKNS
160 170 180 190 200
DEEAPKTAQK KLKLVRTSPE YGMPSVTFGS VHPSDVLDMP VDPNEPTYCL
210 220 230 240
CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP RCSQERKKK
The sequence of this isoform differs from the canonical sequence as follows:
131-131: K → S
132-132: Missing.
10 20 30 40 50
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKGKK SRTQKEKKAA RARSKGKNSD
160 170 180 190 200
EEAPKTAQKK LKLVRTSPEY GMPSVTFGSV HPSDVLDMPV DPNEPTYCLC
210 220 230 240
HQVSYGEMIG CDNPDCSIEW FHFACVGLTT KPRGKWFCPR CSQERKKK
The sequence of this isoform differs from the canonical sequence as follows:
13-37: SIENLPFELQRNFQLMRDLDQRTED → N
10 20 30 40 50
MAAGMYLEHY LDNLKAEIDK LATEYMSSAR SLSSEEKLAL LKQIQEAYGK
60 70 80 90 100
CKEFGDDKVQ LAMQTYEMVD KHIRRLDTDL ARFEADLKEK QIESSDYDSS
110 120 130 140 150
SSKGKKKGRT QKEKKAARAR SKGKNSDEEA PKTAQKKLKL VRTSPEYGMP
160 170 180 190 200
SVTFGSVHPS DVLDMPVDPN EPTYCLCHQV SYGEMIGCDN PDCSIEWFHF
210 220
ACVGLTTKPR GKWFCPRCSQ ERKKK
The sequence of this isoform differs from the canonical sequence as follows:
129-132: Missing.
10 20 30 40 50
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKGRT QKEKKAARAR SKGKNSDEEA
160 170 180 190 200
PKTAQKKLKL VRTSPEYGMP SVTFGSVHPS DVLDMPVDPN EPTYCLCHQV
210 220 230 240
SYGEMIGCDN PDCSIEWFHF ACVGLTTKPR GKWFCPRCSQ ERKKK
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
- Ref.15"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112; LYS-127; LYS-146; LYS-148 AND LYS-156, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114 AND LYS-127 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
The sequence of this isoform differs from the canonical sequence as follows:
128-131: GKKK → E
10 20 30 40 50
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKEGR TQKEKKAARA RSKGKNSDEE
160 170 180 190 200
APKTAQKKLK LVRTSPEYGM PSVTFGSVHP SDVLDMPVDP NEPTYCLCHQ
210 220 230 240
VSYGEMIGCD NPDCSIEWFH FACVGLTTKP RGKWFCPRCS QERKKK
The sequence of this isoform differs from the canonical sequence as follows:
131-131: Missing.
10 20 30 40 50
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKGKK GRTQKEKKAA RARSKGKNSD
160 170 180 190 200
EEAPKTAQKK LKLVRTSPEY GMPSVTFGSV HPSDVLDMPV DPNEPTYCLC
210 220 230 240
HQVSYGEMIG CDNPDCSIEW FHFACVGLTT KPRGKWFCPR CSQERKKK
The sequence of this isoform differs from the canonical sequence as follows:
128-130: Missing.
10 20 30 40 50
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKKGR TQKEKKAARA RSKGKNSDEE
160 170 180 190 200
APKTAQKKLK LVRTSPEYGM PSVTFGSVHP SDVLDMPVDP NEPTYCLCHQ
210 220 230 240
VSYGEMIGCD NPDCSIEWFH FACVGLTTKP RGKWFCPRCS QERKKK
The sequence of this isoform differs from the canonical sequence as follows:
168-249: SPEYGMPSVT...PRCSQERKKK → VPLSGSILPVWG
10 20 30 40 50
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM
60 70 80 90 100
SSARSLSSEE KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL
110 120 130 140 150
DTDLARFEAD LKEKQIESSD YDSSSSKGKK KGRTQKEKKA ARARSKGKNS
160 170
DEEAPKTAQK KLKLVRTVPL SGSILPVWG
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041288 | 13 – 37 | SIENL…QRTED → N in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 25 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041289 | 128 – 131 | GKKK → E in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 4 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041290 | 128 – 130 | Missing in isoform 7. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 3 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041291 | 129 – 132 | Missing in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 4 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012518 | 131 | K → S in isoform 2. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041292 | 131 | Missing in isoform 6. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012519 | 132 | Missing in isoform 2. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041293 | 168 – 249 | SPEYG…ERKKK → VPLSGSILPVWG in isoform 8. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 82 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF156552 mRNA Translation: AAL79773.1 AB197695 mRNA Translation: BAF30477.1 AB197696 mRNA Translation: BAF30478.1 AB197697 mRNA Translation: BAF30479.1 EF152349 mRNA Translation: ABO61139.1 EF152351 mRNA Translation: ABO61141.1 AF063594 mRNA Translation: AAG43153.1 Frameshift. AF110645 mRNA Translation: AAD48585.1 CH471116 Genomic DNA Translation: EAW88763.1 CH471116 Genomic DNA Translation: EAW88768.1 CH471116 Genomic DNA Translation: EAW88770.1 CH471116 Genomic DNA Translation: EAW88772.1 BC007781 mRNA Translation: AAH07781.1 BC013038 mRNA Translation: AAH13038.2 BC095434 mRNA Translation: AAH95434.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS44812.1 [Q9UNL4-3] CCDS44813.1 [Q9UNL4-1] CCDS44814.1 [Q9UNL4-5] CCDS44815.1 [Q9UNL4-4] CCDS44816.1 [Q9UNL4-8] CCDS8555.1 [Q9UNL4-2] |
NCBI Reference Sequences More...RefSeqi | NP_001121054.1, NM_001127582.1 [Q9UNL4-1] NP_001121055.1, NM_001127583.1 [Q9UNL4-5] NP_001121056.1, NM_001127584.1 [Q9UNL4-4] NP_001121057.1, NM_001127585.1 [Q9UNL4-3] NP_001121058.1, NM_001127586.1 [Q9UNL4-8] NP_057246.2, NM_016162.3 [Q9UNL4-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.524210 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000341550; ENSP00000343396; ENSG00000111653 [Q9UNL4-2] ENST00000396807; ENSP00000380024; ENSG00000111653 [Q9UNL4-1] ENST00000412586; ENSP00000412705; ENSG00000111653 [Q9UNL4-5] ENST00000423703; ENSP00000414008; ENSG00000111653 [Q9UNL4-8] ENST00000444704; ENSP00000397343; ENSG00000111653 [Q9UNL4-3] ENST00000446105; ENSP00000415903; ENSG00000111653 [Q9UNL4-4] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 51147 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:51147 |
UCSC genome browser More...UCSCi | uc001qpv.5 human [Q9UNL4-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9UNL4 | Inhibitor of growth protein | 249 | |||
| Inhibitor of growth protein | 249 | ||||
| Inhibitor of growth protein | 249 | ||||
| Inhibitor of growth protein | 249 | ||||
| Inhibitor of growth protein | 249 | ||||
| +248 | |||||
| Q9UNL4-3 | Inhibitor of growth protein | 234 | |||
| UPI0004BE5A01 | 280 | ||||
| UPI000522A507 | 276 | ||||
| UPI0003870093 | 244 | ||||
| UPI000388A1D2 | 259 | ||||
| +58 | |||||
| Q9UNL4-8 | UPI00032AE1C7 | 183 | |||
| ING4 isoform 13 | 179 | ||||
| Inhibitor of growth family member 4 | 179 | ||||
| Inhibitor of growth family member 4 | 179 | ||||
| inhibitor of growth protein 4 isoform X7 | 179 | ||||
| +43 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9UNL4 | Inhibitor of growth protein | 249 | |||
| Inhibitor of growth protein | 249 | ||||
| Inhibitor of growth protein | 249 | ||||
| Inhibitor of growth protein | 249 | ||||
| Inhibitor of growth protein | 249 | ||||
| +534 | |||||
| Q9UNL4-8 | UPI00032AE1C7 | 183 | |||
| Inhibitor of growth family member 4 | 179 | ||||
| inhibitor of growth protein 4 isoform X6 | 179 | ||||
| UPI000441A60D | 179 | ||||
| UPI000A30A95A | 179 | ||||
| +54 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF156552 mRNA Translation: AAL79773.1 AB197695 mRNA Translation: BAF30477.1 AB197696 mRNA Translation: BAF30478.1 AB197697 mRNA Translation: BAF30479.1 EF152349 mRNA Translation: ABO61139.1 EF152351 mRNA Translation: ABO61141.1 AF063594 mRNA Translation: AAG43153.1 Frameshift. AF110645 mRNA Translation: AAD48585.1 CH471116 Genomic DNA Translation: EAW88763.1 CH471116 Genomic DNA Translation: EAW88768.1 CH471116 Genomic DNA Translation: EAW88770.1 CH471116 Genomic DNA Translation: EAW88772.1 BC007781 mRNA Translation: AAH07781.1 BC013038 mRNA Translation: AAH13038.2 BC095434 mRNA Translation: AAH95434.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS44812.1 [Q9UNL4-3] CCDS44813.1 [Q9UNL4-1] CCDS44814.1 [Q9UNL4-5] CCDS44815.1 [Q9UNL4-4] CCDS44816.1 [Q9UNL4-8] CCDS8555.1 [Q9UNL4-2] |
NCBI Reference Sequences More...RefSeqi | NP_001121054.1, NM_001127582.1 [Q9UNL4-1] NP_001121055.1, NM_001127583.1 [Q9UNL4-5] NP_001121056.1, NM_001127584.1 [Q9UNL4-4] NP_001121057.1, NM_001127585.1 [Q9UNL4-3] NP_001121058.1, NM_001127586.1 [Q9UNL4-8] NP_057246.2, NM_016162.3 [Q9UNL4-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.524210 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2K1J | NMR | - | A | 188-249 | [»] | |
| 2M1R | NMR | - | A | 188-249 | [»] | |
| 2PNX | X-ray | 1.80 | A/C | 194-246 | [»] | |
| 2VNF | X-ray | 1.76 | A/C | 188-246 | [»] | |
| 4AFL | X-ray | 2.28 | A/B/C/D/E/F | 2-105 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UNL4 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UNL4 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 119331, 47 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-718 HBO1-4.1 histone acetyltransferase complex CPX-719 HBO1-4.2 histone acetyltransferase complex CPX-720 HBO1-4.3 histone acetyltransferase complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9UNL4 |
Database of interacting proteins More...DIPi | DIP-42222N |
Protein interaction database and analysis system More...IntActi | Q9UNL4, 30 interactors |
Molecular INTeraction database More...MINTi | Q9UNL4 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000380024 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UNL4 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UNL4 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ING4 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 57012981 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9UNL4 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UNL4 |
PeptideAtlas More...PeptideAtlasi | Q9UNL4 |
PRoteomics IDEntifications database More...PRIDEi | Q9UNL4 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 85303 85304 [Q9UNL4-2] 85305 [Q9UNL4-3] 85306 [Q9UNL4-4] 85307 [Q9UNL4-5] 85308 [Q9UNL4-6] 85309 [Q9UNL4-7] 85310 [Q9UNL4-8] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 51147 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000341550; ENSP00000343396; ENSG00000111653 [Q9UNL4-2] ENST00000396807; ENSP00000380024; ENSG00000111653 [Q9UNL4-1] ENST00000412586; ENSP00000412705; ENSG00000111653 [Q9UNL4-5] ENST00000423703; ENSP00000414008; ENSG00000111653 [Q9UNL4-8] ENST00000444704; ENSP00000397343; ENSG00000111653 [Q9UNL4-3] ENST00000446105; ENSP00000415903; ENSG00000111653 [Q9UNL4-4] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 51147 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:51147 |
UCSC genome browser More...UCSCi | uc001qpv.5 human [Q9UNL4-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 51147 |
DisGeNET More...DisGeNETi | 51147 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000111653.19 |
GeneCards: human genes, protein and diseases More...GeneCardsi | ING4 |
Human Gene Nomenclature Database More...HGNCi | HGNC:19423 ING4 |
Human Protein Atlas More...HPAi | HPA031817 HPA057338 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 608524 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UNL4 |
Open Targets More...OpenTargetsi | ENSG00000111653 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134976283 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1973 Eukaryota COG5034 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000074538 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000239724 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG006607 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UNL4 |
KEGG Orthology (KO) More...KOi | K11346 |
Identification of Orthologs from Complete Genome Data More...OMAi | PRCSQDR |
Database of Orthologous Groups More...OrthoDBi | EOG091G0J8Y |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UNL4 |
TreeFam database of animal gene trees More...TreeFami | TF352014 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-3214847 HATs acetylate histones |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9UNL4 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | ING4 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9UNL4 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | ING4 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 51147 |
Protein Ontology More...PROi | PR:Q9UNL4 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000111653 |
CleanEx database of gene expression profiles More...CleanExi | HS_ING4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UNL4 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UNL4 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.40.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR028647 ING4 IPR024610 ING_N_histone_binding IPR019786 Zinc_finger_PHD-type_CS IPR011011 Znf_FYVE_PHD IPR001965 Znf_PHD IPR019787 Znf_PHD-finger IPR013083 Znf_RING/FYVE/PHD |
The PANTHER Classification System More...PANTHERi | PTHR10333:SF40 PTHR10333:SF40, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF12998 ING, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01408 ING, 1 hit SM00249 PHD, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF57903 SSF57903, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01359 ZF_PHD_1, 1 hit PS50016 ZF_PHD_2, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | ING4_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q9UNL4Primary (citable) accession number: Q9UNL4 Secondary accession number(s): A4KYM4 , A4KYM6, D3DUR8, Q0EF62, Q0EF63, Q4VBQ6, Q96E15, Q9H3J0 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 4, 2005 |
| Last sequence update: | May 1, 2000 | |
| Last modified: | July 18, 2018 | |
| This is version 165 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
